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Dynamics of Protein–ssDNA Interactions in the Bacteriophage T4 Homologous Recombination System

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Biophysics of DNA-Protein Interactions

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Abstract

Homologous recombination plays critical roles in maintaining genetic diversity and genome stability through processes such as meiosis and DNA double-strand break repair. The central process in homologous recombination is DNA strand exchange, in which single-stranded DNA (ssDNA) from the resected, broken end of one chromosome invades the homologous double-stranded DNA (dsDNA) of a sister chromosome. This reaction is catalyzed by presynaptic filaments – filamentous complexes of core recombination proteins bound to the invading ssDNA. Successful recombination depends on the coordinated assembly and dynamics of these protein–ssDNA filaments. Studies of the bacteriophage T4 core recombination machinery (UvsX recombinase, Gp32 ssDNA-binding protein, UvsY recombination mediator protein) have provided valuable insights on the biochemistry and biophysics of protein–ssDNA interactions in homologous recombination. In this chapter, we explore current models for the assembly and dynamic instability of the T4 presynaptic filament and show how mechanistic features of this system may be conserved in other recombination systems.

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  1. Department of Biochemistry, University of Vermont College of Medicine, Burlington, VT, 05405, USA

    Scott W. Morrical

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  1. Dept. Physics, Northeastern University, Forsyth Street 110, Boston, 02115, Massachusetts, USA

    Mark C. Williams

  2. College of Medicine, Dept. Biochemistry & Molecular Biology, Mayo Clinic, First Street SW., 200, Rochester, 55905, Minnesota, USA

    L. James Maher III

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Liu, J., Morrical, S.W. (2010). Dynamics of Protein–ssDNA Interactions in the Bacteriophage T4 Homologous Recombination System. In: Williams, M., Maher, L. (eds) Biophysics of DNA-Protein Interactions. Biological and Medical Physics, Biomedical Engineering. Springer, New York, NY. https://doi.org/10.1007/978-0-387-92808-1_10

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